Jones, DT; Uppenbrink, J; Pearl, LH; Thornton, JM; Moody, CM; Doyle, PM; ... Sadler, PJ; + view all Jones, DT; Uppenbrink, J; Pearl, LH; Thornton, JM; Moody, CM; Doyle, PM; Harris, CJ; Viles, JH; Sadler, PJ; - view fewer (1996) Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein. Proteins: Structure, Function and Genetics , 24 (4) 502 - 513. 10.1002/(SICI)1097-0134(199604)24:4<502::AID-PROT9>3.0.CO;2-F.
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In response to the Paracelsus Challenge (Rose and Creamer, Proteins, 19:1- 3, 1994), we present here the design, synthesis, and characterization of a helical protein, whose sequence is 50% identical to that of an all-β protein. The new sequence was derived by applying an inverse protein folding approach, in which the sequence was optimized to 'fit' the new helical structure, but constrained to retain 50% of the original amino acid residues. The program utilizes a genetic algorithm to optimize the sequence, together with empirical potentials of mean force to evaluate the sequence-structure compatibility. Although the designed sequence has little ordered (secondary) structure in water, circular dichroism and nuclear magnetic resonance data show clear evidence for significant helical content in water/ethylene glycol and in water/methanol mixtures at low temperatures, as well as melting behavior indicative of cooperative folding. We believe that this represents a significant step toward meeting the Paracelsus Challenge.
|Title:||Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein|
|UCL classification:||UCL > School of BEAMS > Faculty of Engineering Science > Computer Science|
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